1dl3

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(New page: 200px<br /><applet load="1dl3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dl3, resolution 2.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dl3.gif|left|200px]]<br /><applet load="1dl3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dl3, resolution 2.7&Aring;" />
 
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'''CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA==
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BACKGROUND: Oligomeric proteins may have been selected for in, hyperthermophiles because subunit association provides extra, stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric, and labile in most mesophilic microorganisms, but dimeric and stable in, the hyperthermophile Thermotoga maritima (tPRAI). The two subunits of, tPRAI are associated back-to-back and are locked together by a hydrophobic, loop. The hypothesis that dimerization is important for thermostability, has been tested by rationally designing monomeric variants of tPRAI., RESULTS: The comparison of tPRAI and PRAI from Escherichia coli (ePRAI), suggested that levelling the nonplanar dimer interface would weaken the, association. The deletion of two residues in the loop loosened the dimer., Subsequent filling of the adjacent pocket and the exchange of polar for, apolar residues yielded a weakly associating and a nonassociating, monomeric variant. Both variants are as active as the parental dimer but, far more thermolabile. The thermostability of the weakly associating, monomer increased significantly with increasing protein concentration. The, X-ray structure of the nonassociating monomer differed from that of the, parental subunit only in the restructured interface. The orientation of, the original subunits was maintained in a crystal contact between two, monomers. CONCLUSIONS: tPRAI is dimeric for reasons of stability. The, clearly separated responsibilities of the betaalpha loops, which are, involved in activity, and the alphabeta loops, which are involved in, protein stability, has permitted the evolution of dimers without, compromising their activity. The preserved interaction in the crystal, contacts suggests the most likely model for dimer evolution.
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<StructureSection load='1dl3' size='340' side='right'caption='[[1dl3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1dl3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DL3 FirstGlance]. <br>
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1DL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DL3 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dl3 OCA], [https://pdbe.org/1dl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dl3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dl3 ProSAT]</span></td></tr>
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Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima., Thoma R, Hennig M, Sterner R, Kirschner K, Structure. 2000 Mar 15;8(3):265-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10745009 10745009]
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</table>
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[[Category: Phosphoribosylanthranilate isomerase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/TRPF_THEMA TRPF_THEMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/1dl3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dl3 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Hennig, M.]]
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[[Category: Hennig M]]
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[[Category: Kirschner, K.]]
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[[Category: Kirschner K]]
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[[Category: Sterner, R.]]
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[[Category: Sterner R]]
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[[Category: Thoma, R.]]
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[[Category: Thoma R]]
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[[Category: SO4]]
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[[Category: dimer evolution]]
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[[Category: isomerase]]
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[[Category: oligomerisation]]
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[[Category: protein engineering]]
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[[Category: thermostability]]
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[[Category: thermotoga maritima]]
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[[Category: x-ray structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:22:48 2007''
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Current revision

CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA

PDB ID 1dl3

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